4IHU

Reduced form of disulfide bond oxdioreductase (DsbG) from Mycobacterium tuberculosis

4IHU の概要

• エントリーDOI: 10.2210/pdb4ihu/pdb
• 分子名称: Isomerase DsbG, CHLORIDE ION (3 entities in total)
• 機能のキーワード: thioredoxin, disulfide bond isomerase, redox, oxidoreductase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47285.93

構造登録者

Harmston, C.A.,Goulding, C.W. (登録日: 2012-12-19, 公開日: 2013-10-30, 最終更新日: 2024-11-20)

主引用文献

Chim, N.,Harmston, C.A.,Guzman, D.J.,Goulding, C.W.
Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis.
Bmc Struct.Biol., 13:23-23, 2013

PubMed Abstract: Bacterial Disulfide bond forming (Dsb) proteins facilitate proper folding and disulfide bond formation of periplasmic and secreted proteins. Previously, we have shown that Mycobacterium tuberculosis Mt-DsbE and Mt-DsbF aid in vitro oxidative folding of proteins. The M. tuberculosis proteome contains another predicted membrane-tethered Dsb protein, Mt-DsbA, which is encoded by an essential gene.

PubMed: 24134223
DOI: 10.1186/1472-6807-13-23

実験手法

X-RAY DIFFRACTION (1.896 Å)